Electrically contacting redox-enzymes to electrodes is a major goal for developing amperometric biosensers,1-3 biofuel cells4-5 and bioelectronic elements.6 Integrated electrically-contacted enzyme-electrodes were prepared by the tethering of an electron mediator group to the enzyme associated with the electrode,7-8 and by the immobilization of redox-enzymes in redox-active polymers assembled on electrodes.9-10 The effectiveness of electron transfer communication in these systems is, however, substantially lower than the electron transfer turnover rates of the enzymes with their native substrates.11 This has been attributed to a random, non-optimal, modification of the redox-proteins by the electroactive relay units, and to the random orientation of the enzymes in respect to the electrode support.3 It was previously demonstrated12-14 that the reconstitution of an apo-flavoenzyme, apo-glucose oxidase (Apo-GOx), on a relay-FAD (flavin adenine dinucleotide) monolayer associated with an electrode yields an aligned, electrically contracted, enzyme-electrode with an unprecedented effective electron transfer communication that is similar to the electron transfer turnover rate of the enzyme with its native substrate (oxygen). This efficient electrical communication between the surface reconstituted bioelectrocatalyst and the electrode was utilized to develop enzyme-electrodes for a glucose sensor,12-14 and for a glucose-base biofuel cell.5 To generate the relay-FAD monolayer in these systems, the covalent coupling of a synthetic aminoethyl-FAD unit to the relay component is a key step. The elaborate synthesis of this cofactor15 turned the approach to be of limited practical utility.